6e8o
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Implication of MbtH-like proteins in crystallization of the independent NRPS A domains. Crystal structure of FscC: supporting rationale for revised mechanism of freestanding aryl acid adenylating enzymes.== | |
| - | + | <StructureSection load='6e8o' size='340' side='right'caption='[[6e8o]], [[Resolution|resolution]] 1.70Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[6e8o]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E8O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E8O FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |
| - | [[Category: | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6e8o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e8o OCA], [http://pdbe.org/6e8o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e8o RCSB], [http://www.ebi.ac.uk/pdbsum/6e8o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e8o ProSAT]</span></td></tr> |
| + | </table> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Bruner, S D]] | ||
| + | [[Category: Zagulyaeva, A A]] | ||
| + | [[Category: Adenylation domain]] | ||
| + | [[Category: Ligase]] | ||
| + | [[Category: Nrp]] | ||
| + | [[Category: Siderophore biosynthesis]] | ||
| + | [[Category: Thiolation state]] | ||
Revision as of 05:49, 21 August 2019
Implication of MbtH-like proteins in crystallization of the independent NRPS A domains. Crystal structure of FscC: supporting rationale for revised mechanism of freestanding aryl acid adenylating enzymes.
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